Anti-ADAM10 Purified

Description: The polyclonal antibody reacts with human, mouse, and rat ADAM10; the antibody was raised against residues 732-748 of human ADAM10, also known as KUZ and MADM. ADAM10 is a member of the ADAM (A Disintegrin And Metalloprotease) family of membrane-anchored glycoproteins comprised of several distinct protein modules, including a pro- and metalloprotease domain, disintegrin domain, cysteine-rich region and an EGF repeat. These proteases perform essential functions in cell adhesion and fusion in diverse systems and participate in ectodomain shedding of molecules such as TNF-α and Drosophila signaling molecule Notch.

References:
Fahrenholz, F., S. Gilbert, et al. 2000. Alpha-secretase activity of the disintegrin metalloprotease ADAM 10. Influences of domain structure. Ann N Y Acad Sci 920: 215-22.
Mullberg, J., K. Althoff, et al. 2000. The importance of shedding of membrane proteins for cytokine biology. Eur Cytokine Netw 11: 27-38.
Stone, A. L., M. Kroeger, et al. 1999. Structure-function analysis of the ADAM family of disintegrin-like and metalloproteinase-containing proteins. J Protein Chem 18: 447-65.
Yamamoto, S., Y. Higuchi, et al. 1999. ADAM family proteins in the immune system. Immunol Today 20: 278-84.
Huovila, A. P., E. A. Almeida, et al. 1996. ADAMs and cell fusion. Curr Opin Cell Biol 8: 692-9.
Wolfsberg, T. G., P. Primakoff, et al. 1995. ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J Cell Biol 131: 275-8.